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8VJ2

Crystal Structure of Macrophage migration inhibitory factor-1 (MIF1) from Onchocerca volvulus

Summary for 8VJ2
Entry DOI10.2210/pdb8vj2/pdb
DescriptorMacrophage migration inhibitory factor-1, SODIUM ION (3 entities in total)
Functional Keywordsssgcid, structural genomics, seattle structural genomics center for infectious disease, macrophage migration inhibitory factor-1, cytokine
Biological sourceOnchocerca volvulus
Total number of polymer chains3
Total formula weight43398.36
Authors
Seattle Structural Genomics Center for Infectious Disease,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2024-01-05, release date: 2024-01-17, Last modification date: 2024-12-18)
Primary citationKimble, A.D.,Dawson, O.C.O.,Liu, L.,Subramanian, S.,Cooper, A.,Battaile, K.,Craig, J.,Harmon, E.,Myler, P.,Lovell, S.,Asojo, O.A.
Crystal structure of N-terminally hexahistidine-tagged Onchocerca volvulus macrophage migration inhibitory factor-1.
Acta Crystallogr.,Sect.F, 80:328-334, 2024
Cited by
PubMed Abstract: Onchocerca volvulus causes blindness, onchocerciasis, skin infections and devastating neurological diseases such as nodding syndrome. New treatments are needed because the currently used drug, ivermectin, is contraindicated in pregnant women and those co-infected with Loa loa. The Seattle Structural Genomics Center for Infectious Disease (SSGCID) produced, crystallized and determined the apo structure of N-terminally hexahistidine-tagged O. volvulus macrophage migration inhibitory factor-1 (His-OvMIF-1). OvMIF-1 is a possible drug target. His-OvMIF-1 has a unique jellyfish-like structure with a prototypical macrophage migration inhibitory factor (MIF) trimer as the `head' and a unique C-terminal `tail'. Deleting the N-terminal tag reveals an OvMIF-1 structure with a larger cavity than that observed in human MIF that can be targeted for drug repurposing and discovery. Removal of the tag will be necessary to determine the actual biological oligomer of OvMIF-1 because size-exclusion chomatographic analysis of His-OvMIF-1 suggests a monomer, while PISA analysis suggests a hexamer stabilized by the unique C-terminal tails.
PubMed: 39503735
DOI: 10.1107/S2053230X24010550
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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